Thiol-activated fluorescent probe for sensitive detection and imaging of proteins

Du, Jianjun; Ma, Weijun; Gu, Quanyong; Yao, Qichao; Long, Saran; Sun, Wen; Fan, Jiangli; Peng, Xiaojun

doi:10.1016/j.snb.2019.02.029

Cited by 19 publications

(5 citation statements)

References 39 publications

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“…Assessment of the binding capacity of albumin is very important in clinical practice as this parameter is crucial for the efficacy of drug therapy. The simplest and the most convenient method for studying the binding capacity of albumin is the use of fluorescent probes. − The proper choice of a fluorescent probe, which should selectively bind to albumin-binding sites, should not change the albumin structure, and should provide high signal at low protein content, is of high importance. For this purpose, a fluorescent probe CAPIDAN (or K-35, N-(p-carboxyphenyl)imide of 4-(dimethylamino)naphthalic acid) has been proposed. − The K-35 fluorescent probe is advantageous due to the high selectivity and specificity of albumin binding, high sensitivity and applicability for the analysis of biological fluids with a low protein content, as well as its nondestructive properties. , Upon interaction with HSA, K-35 molecules occupy the binding sites of four types. ,, 90–95% of K-35 fluorescence in blood plasma is due to its binding to albumin. − If any of the sites lose their binding capacity, the amount of K-35 capable of interaction with HSA decreases, which results in the decrease in the intensity of the characteristic fluorescence.…”

Section: Resultsmentioning

confidence: 99%

Albumin Retains Its Transport Function after Interaction with Cerium Dioxide Nanoparticles

Sozarukova,

Kochneva,

Proskurnina

et al. 2023

ACS Biomater. Sci. Eng.

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The interaction of inorganic nanomaterials with biological fluids containing proteins can lead not only to the formation of a protein corona and thereby to a change in the biological activity of nanoparticles but also to a significant effect on the structural and functional properties of the biomolecules themselves. This work studied the interaction of nanoscale CeO 2 , the most versatile nanozyme, with human serum albumin (HSA). Fourier transform infrared spectroscopy, MALDI-TOF mass spectrometry, UV−vis spectroscopy, and fluorescence spectroscopy confirmed the formation of HSA-CeO 2 nanoparticle conjugates. Changes in protein conformation, which depend on the concentration of both citrate-stabilized CeO 2 nanoparticles and pristine CeO 2 nanoparticles, did not affect albumin drug-binding sites and, accordingly, did not impair the HSA transport function.The results obtained shed light on the biological consequences of the CeO 2 nanoparticles' entrance into the body, which should be taken into account when engineering nanobiomaterials to increase their efficiency and reduce the side effects.

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Section: Resultsmentioning

confidence: 99%

Albumin Retains Its Transport Function after Interaction with Cerium Dioxide Nanoparticles

Sozarukova,

Kochneva,

Proskurnina

et al. 2023

ACS Biomater. Sci. Eng.

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“…Previous studies from our group and others have shown that solvatochromic dyes (also known as environment-sensitive dyes) are particularly useful in constructing protein probes. − These probes have low fluorescence in aqueous solutions but display strong emission once they bind to proteins due to the alteration of the microenvironment of the probes. Thus, herein, we reasoned that decoration of solvatochromic fluorophores with a disulfide-reactive group may generate selective off–on fluorescent probes of PDS.…”

Section: Resultsmentioning

confidence: 99%

Fluorescent Probes for Imaging Protein Disulfides in Live Organisms

Zhong

Zhao

et al. 2021

ACS Sens.

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Cellular redox homeostasis is predominantly controlled by the ratio of thiols and disulfides, and reversible thiol-disulfide exchange reactions are fundamental of the biological redox regulation. However, due to the dynamic exchanges of thiols and disulfides, the detection, especially the in situ detection, of protein disulfides (PDS) is challenging. We employ the strategy, i.e., the increase of emission upon an environment-sensitive dye binding to proteins, to design PDS probes and discover a two-photon probe PDSTP590 (S6) that selectively recognizes PDS in live organisms. With the aid of the probe, we further disclose the elevation of PDS in brains of the mouse stroke model.

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“…The performance of probes 68 – 78 − in detecting albumin was also excellent. Experiments showed that fluorescent probe 68 had the potential to diagnosis cancer (Figure ).…”

Section: Fluorescence Probes For Qualitative and Quantitative Hsamentioning

confidence: 91%

“…104 Probe 71 could identify specific proteins containing free cysteine residues. 105 In addition to being used for quantitatively detecting trace HSA in urine and serum, it also realized the HSA imaging of human breast cancer cells. The detection of albumin by probe 72 could be realized immediately after addition, 106 which could be used for actual serum detection and cell imaging.…”

Section: Detection Of Hsa Based On Spatialmentioning

confidence: 99%

“…NIR fluorescent probe 70 showed a 500-fold fluorescence enhancement after reacting with albumin . Probe 71 could identify specific proteins containing free cysteine residues . In addition to being used for quantitatively detecting trace HSA in urine and serum, it also realized the HSA imaging of human breast cancer cells.…”

Section: Fluorescence Probes For Qualitative and Quantitative Hsamentioning

confidence: 99%

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Development of Human Serum Albumin Fluorescent Probes in Detection, Imaging, and Disease Therapy

Wang,

Huo,

Yin

2024

J. Phys. Chem. B

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Human serum albumin (HSA) acts as a repository and transporter of substances in the blood. An abnormal concentration may indicate the occurrence of liver-and kidney-related diseases, which has attracted people to investigate the precise quantification of HSA in body fluids. Fluorescent probes can combine with HSA covalently or noncovalently to quantify HSA in urine and plasma. Moreover, probes combined with HSA can improve its photophysical properties; probe-HSA has been applied in real-time monitoring and photothermal and photodynamic therapy in vivo. This Review will introduce fluorescent probes for quantitative HSA according to the three reaction mechanisms of spatial structure, enzymatic reaction, and self-assembly and systematically introduce the application of probes combined with HSA in disease imaging and phototherapy. It will help develop multifunctional applications for HSA probes and provide assistance in the early diagnosis and treatment of diseases.

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Thiol-activated fluorescent probe for sensitive detection and imaging of proteins

Cited by 19 publications

References 39 publications

Albumin Retains Its Transport Function after Interaction with Cerium Dioxide Nanoparticles

Albumin Retains Its Transport Function after Interaction with Cerium Dioxide Nanoparticles

Fluorescent Probes for Imaging Protein Disulfides in Live Organisms

Development of Human Serum Albumin Fluorescent Probes in Detection, Imaging, and Disease Therapy

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